The main goal of this proposal is to characterize the components of the motility and chemotaxis system. By determining the properties of the components, we will be able to reconstruct the events involved in these phenomena. We propose to study bacterial motility and chemotaxis by combining biochemical and genetic techniques. Specifically, we will use recombinant DNA technology to analytically dissect the system into its component parts. This approach is not only unique to this problem but it offers a means of studying motility and chemotaxis which is not possible by biochemical or genetic techniques alone. Two of the major problems of biochemiocal characterization has been the lack of a means to purify these proteins and the low level of expression. We have solved these problems by raising antibodies against one of the chemotaxis proteins and have subcloned the motility and chemotaxis genes onto vehicles which enhanced levels of expression. Once we have purified the components using the above techniques, we will study these proteins biochemically. From preliminary observations, we feel that some components may interact with S-adenosylmethionine. We also propose to probe the nature of the integral membrane proteins involved in motility by again exploiting recombinant DNA technology. First, we propose to sequence the motA gene. Using the DNA sequence of the motA gene and the concomitant amino acid sequence of the motA gene product, we will in vitro synthesize small (10-12 amino acids) peptides which will be used to raise antibody to predetermined areas of the motA protein. These specific probes will be used to determine the arrangement and the molecular architecture of the motA gene product in the membrane.